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2qjy

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[[Image:2qjy.jpg|left|200px]]<br /><applet load="2qjy" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2qjy, resolution 2.40&Aring;" />
 
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'''Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2'''<br />
 
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==Overview==
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==Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2==
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<StructureSection load='2qjy' size='340' side='right'caption='[[2qjy]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2qjy]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Cereibacter_sphaeroides Cereibacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QJY FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGL:B-2-OCTYLGLUCOSIDE'>BGL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LOP:(1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL+(9Z)-OCTADEC-9-ENOATE'>LOP</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SMA:STIGMATELLIN+A'>SMA</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene>, <scene name='pdbligand=UQ2:UBIQUINONE-2'>UQ2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qjy OCA], [https://pdbe.org/2qjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qjy RCSB], [https://www.ebi.ac.uk/pdbsum/2qjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qjy ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CYB_CERSP CYB_CERSP] Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qj/2qjy_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2qjy ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
The cytochrome bc(1) complex (bc(1)) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc(1) complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor stigmatellin alone or in combination with the quinone reduction (Q(N)) site inhibitor antimycin, were determined. The high quality electron density permitted assignments of a new metal-binding site to the cytochrome c(1) subunit and a number of lipid and detergent molecules. Structural differences between Rsbc(1) and its mitochondrial counterparts are mostly extra membranous and provide a basis for understanding the function of the predominantly longer sequences in the bacterial subunits. Functional implications for the bc(1) complex are derived from analyses of 10 independent molecules in various crystal forms and from comparisons with mitochondrial complexes.
The cytochrome bc(1) complex (bc(1)) is a major contributor to the proton motive force across the membrane by coupling electron transfer to proton translocation. The crystal structures of wild type and mutant bc(1) complexes from the photosynthetic purple bacterium Rhodobacter sphaeroides (Rsbc(1)), stabilized with the quinol oxidation (Q(P)) site inhibitor stigmatellin alone or in combination with the quinone reduction (Q(N)) site inhibitor antimycin, were determined. The high quality electron density permitted assignments of a new metal-binding site to the cytochrome c(1) subunit and a number of lipid and detergent molecules. Structural differences between Rsbc(1) and its mitochondrial counterparts are mostly extra membranous and provide a basis for understanding the function of the predominantly longer sequences in the bacterial subunits. Functional implications for the bc(1) complex are derived from analyses of 10 independent molecules in various crystal forms and from comparisons with mitochondrial complexes.
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==About this Structure==
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Inhibitor-complexed structures of the cytochrome bc1 from the photosynthetic bacterium Rhodobacter sphaeroides.,Esser L, Elberry M, Zhou F, Yu CA, Yu L, Xia D J Biol Chem. 2008 Feb 1;283(5):2846-57. Epub 2007 Nov 26. PMID:18039651<ref>PMID:18039651</ref>
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2QJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=BGL:'>BGL</scene>, <scene name='pdbligand=SR:'>SR</scene>, <scene name='pdbligand=CL:'>CL</scene>, <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=HEM:'>HEM</scene>, <scene name='pdbligand=SMA:'>SMA</scene>, <scene name='pdbligand=LOP:'>LOP</scene>, <scene name='pdbligand=UQ2:'>UQ2</scene> and <scene name='pdbligand=FES:'>FES</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Ubiquinol--cytochrome-c_reductase Ubiquinol--cytochrome-c reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.10.2.2 1.10.2.2] Known structural/functional Sites: <scene name='pdbsite=AC1:Bgl+Binding+Site+For+Residue+B+1041'>AC1</scene>, <scene name='pdbsite=AC2:Bgl+Binding+Site+For+Residue+E+1042'>AC2</scene>, <scene name='pdbsite=AC3:Bgl+Binding+Site+For+Residue+G+1043'>AC3</scene>, <scene name='pdbsite=AC4:Bgl+Binding+Site+For+Residue+K+1044'>AC4</scene>, <scene name='pdbsite=AC5:Bgl+Binding+Site+For+Residue+N+1045'>AC5</scene>, <scene name='pdbsite=AC6:Bgl+Binding+Site+For+Residue+P+1046'>AC6</scene>, <scene name='pdbsite=AC7:Sr+Binding+Site+For+Residue+B+1011'>AC7</scene>, <scene name='pdbsite=AC8:Sr+Binding+Site+For+Residue+E+1012'>AC8</scene>, <scene name='pdbsite=AC9:Sr+Binding+Site+For+Residue+H+1013'>AC9</scene>, <scene name='pdbsite=BC1:Sr+Binding+Site+For+Residue+K+1014'>BC1</scene>, <scene name='pdbsite=BC2:Sr+Binding+Site+For+Residue+N+1015'>BC2</scene>, <scene name='pdbsite=BC3:Sr+Binding+Site+For+Residue+Q+1016'>BC3</scene>, <scene name='pdbsite=BC4:Na+Binding+Site+For+Residue+R+2001'>BC4</scene>, <scene name='pdbsite=BC5:Cl+Binding+Site+For+Residue+I+2004'>BC5</scene>, <scene name='pdbsite=BC6:Cl+Binding+Site+For+Residue+R+2005'>BC6</scene>, <scene name='pdbsite=BC7:Hem+Binding+Site+For+Residue+A+501'>BC7</scene>, <scene name='pdbsite=BC8:Hem+Binding+Site+For+Residue+A+502'>BC8</scene>, <scene name='pdbsite=BC9:Hem+Binding+Site+For+Residue+B+301'>BC9</scene>, <scene name='pdbsite=CC1:Fes+Binding+Site+For+Residue+C+200'>CC1</scene>, <scene name='pdbsite=CC2:Hem+Binding+Site+For+Residue+D+501'>CC2</scene>, <scene name='pdbsite=CC3:Hem+Binding+Site+For+Residue+D+502'>CC3</scene>, <scene name='pdbsite=CC4:Hem+Binding+Site+For+Residue+E+301'>CC4</scene>, <scene name='pdbsite=CC5:Fes+Binding+Site+For+Residue+F+200'>CC5</scene>, <scene name='pdbsite=CC6:Hem+Binding+Site+For+Residue+G+501'>CC6</scene>, <scene name='pdbsite=CC7:Hem+Binding+Site+For+Residue+G+502'>CC7</scene>, <scene name='pdbsite=CC8:Hem+Binding+Site+For+Residue+H+301'>CC8</scene>, <scene name='pdbsite=CC9:Fes+Binding+Site+For+Residue+I+200'>CC9</scene>, <scene name='pdbsite=DC1:Hem+Binding+Site+For+Residue+J+501'>DC1</scene>, <scene name='pdbsite=DC2:Hem+Binding+Site+For+Residue+J+502'>DC2</scene>, <scene name='pdbsite=DC3:Hem+Binding+Site+For+Residue+K+301'>DC3</scene>, <scene name='pdbsite=DC4:Fes+Binding+Site+For+Residue+L+200'>DC4</scene>, <scene name='pdbsite=DC5:Hem+Binding+Site+For+Residue+M+501'>DC5</scene>, <scene name='pdbsite=DC6:Hem+Binding+Site+For+Residue+M+502'>DC6</scene>, <scene name='pdbsite=DC7:Hem+Binding+Site+For+Residue+N+301'>DC7</scene>, <scene name='pdbsite=DC8:Fes+Binding+Site+For+Residue+O+200'>DC8</scene>, <scene name='pdbsite=DC9:Hem+Binding+Site+For+Residue+P+501'>DC9</scene>, <scene name='pdbsite=EC1:Hem+Binding+Site+For+Residue+P+502'>EC1</scene>, <scene name='pdbsite=EC2:Hem+Binding+Site+For+Residue+Q+301'>EC2</scene>, <scene name='pdbsite=EC3:Fes+Binding+Site+For+Residue+R+200'>EC3</scene>, <scene name='pdbsite=EC4:Sma+Binding+Site+For+Residue+A+1001'>EC4</scene>, <scene name='pdbsite=EC5:Sma+Binding+Site+For+Residue+D+1002'>EC5</scene>, <scene name='pdbsite=EC6:Sma+Binding+Site+For+Residue+G+1003'>EC6</scene>, <scene name='pdbsite=EC7:Sma+Binding+Site+For+Residue+J+1004'>EC7</scene>, <scene name='pdbsite=EC8:Sma+Binding+Site+For+Residue+M+1005'>EC8</scene>, <scene name='pdbsite=EC9:Sma+Binding+Site+For+Residue+P+1006'>EC9</scene>, <scene name='pdbsite=FC1:Lop+Binding+Site+For+Residue+A+1021'>FC1</scene>, <scene name='pdbsite=FC2:Lop+Binding+Site+For+Residue+D+1022'>FC2</scene>, <scene name='pdbsite=FC3:Lop+Binding+Site+For+Residue+G+1023'>FC3</scene>, <scene name='pdbsite=FC4:Lop+Binding+Site+For+Residue+J+1024'>FC4</scene>, <scene name='pdbsite=FC5:Lop+Binding+Site+For+Residue+M+1025'>FC5</scene>, <scene name='pdbsite=FC6:Lop+Binding+Site+For+Residue+P+1026'>FC6</scene>, <scene name='pdbsite=FC7:Uq2+Binding+Site+For+Residue+A+1101'>FC7</scene>, <scene name='pdbsite=FC8:Uq2+Binding+Site+For+Residue+D+1102'>FC8</scene>, <scene name='pdbsite=FC9:Uq2+Binding+Site+For+Residue+G+1103'>FC9</scene>, <scene name='pdbsite=GC1:Uq2+Binding+Site+For+Residue+J+1104'>GC1</scene>, <scene name='pdbsite=GC2:Uq2+Binding+Site+For+Residue+M+1105'>GC2</scene> and <scene name='pdbsite=GC3:Uq2+Binding+Site+For+Residue+P+1106'>GC3</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QJY OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Inhibitor-complexed Structures of the Cytochrome bc1 from the Photosynthetic Bacterium Rhodobacter sphaeroides., Esser L, Elberry M, Zhou F, Yu CA, Yu L, Xia D, J Biol Chem. 2008 Feb 1;283(5):2846-57. Epub 2007 Nov 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18039651 18039651]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 2qjy" style="background-color:#fffaf0;"></div>
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[[Category: Rhodobacter sphaeroides]]
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[[Category: Ubiquinol--cytochrome-c reductase]]
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[[Category: Esser, L.]]
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[[Category: Xia, D.]]
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[[Category: BGL]]
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[[Category: CL]]
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[[Category: FES]]
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[[Category: HEM]]
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[[Category: LOP]]
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[[Category: NA]]
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[[Category: SMA]]
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[[Category: SR]]
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[[Category: UQ2]]
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[[Category: 1 c-term tm helix rieske]]
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[[Category: 1 n-term tm helix]]
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[[Category: 8 tm helixces cytochrome c1]]
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[[Category: cytochrome b]]
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[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:39:57 2008''
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==See Also==
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*[[Cytochrome C 3D structures|Cytochrome C 3D structures]]
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*[[Cytochrome bc1 3D structures|Cytochrome bc1 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Cereibacter sphaeroides]]
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[[Category: Large Structures]]
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[[Category: Esser L]]
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[[Category: Xia D]]

Current revision

Crystal structure of rhodobacter sphaeroides double mutant with stigmatellin and UQ2

PDB ID 2qjy

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